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Database: UniProt
Entry: A0A1M5AUW8_9BACT
LinkDB: A0A1M5AUW8_9BACT
Original site: A0A1M5AUW8_9BACT 
ID   A0A1M5AUW8_9BACT        Unreviewed;       914 AA.
AC   A0A1M5AUW8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444008_10718 {ECO:0000313|EMBL:SHF34024.1};
OS   Cnuella takakiae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Cnuella.
OX   NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHF34024.1, ECO:0000313|Proteomes:UP000184368};
RN   [1] {ECO:0000313|EMBL:SHF34024.1, ECO:0000313|Proteomes:UP000184368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26897 {ECO:0000313|EMBL:SHF34024.1,
RC   ECO:0000313|Proteomes:UP000184368};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; FQUO01000007; SHF34024.1; -; Genomic_DNA.
DR   RefSeq; WP_073042713.1; NZ_MTFE01000010.1.
DR   AlphaFoldDB; A0A1M5AUW8; -.
DR   STRING; 1302690.BUE76_16085; -.
DR   OrthoDB; 607558at2; -.
DR   Proteomes; UP000184368; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 5.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 3.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 5.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184368}.
FT   DOMAIN          86..139
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          140..211
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          213..265
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          602..654
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          683..911
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          649..683
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   914 AA;  105955 MW;  EB3C00E5E2EADB26 CRC64;
     MLIGKNAQIE SERLKTALEA AGVGVWDYDL VRDELVWSLH CYRLFGITDP FPMSFDIFLS
     GLHPLDRERT KEVVQHAFNP ESGGTYDIEY RTVGIQDGIT RWVRATGKAY FDATGKAYRF
     VGTIADISAQ KEAEAQLQES EARFRNMADS APVMIWITDP NGHCNYLNLR WLEFTGQTME
     EGSGIGWADA VHPDDRHKTK EAFVASNTEK RAFRVEYRLR SKSGQYRWML DSALPRFDEA
     GRFLGYIGSV LDISDRKQTE EELQFRTAQL EAQNEATEYG LLLVDTKGKI LSQNKRFSEM
     WHMPQEIIDS KDDNRALEHA QTMVQEPEQF IRRVKDRYES NMEVASDEFR FKDGRIIERT
     GRPVTGKDGM HYGYLWQFRD ITAYRAAQDA LELRTALLEA QNEASPLGIL VIDQNYKFNY
     FNKGYVKVFD LPQEVVANPS REALLGYFEQ TIINYEAFNE RITYLYNNPV SGSLDEVYLK
     NGKIIERYGY PIRGKEGRYF GWTWQFRDIT EERRYQEYME QKNRQLETLI QEFKFVTDFM
     PQMVWATQPD GYHDFFNKQW YDYTGLDYET TKDKGWSLVL HPDDSERTWQ VWHHSLETGA
     IYQIEYRMRR YDGVYRWMLG RAIPMRDAAG TIIKWFGTCT DIDDQRRSAE LLEQKVAERT
     RDLQEANENL ERSNAELEQF AYVASHDLQE PLRKIRTFTT MLEGELQRGD LHKSKSYIER
     IWQSSSRMQE LIRDLLDFSR LNQSEPAAFE LVDLNTIAKN IIGDLELSIA QKGAEVHIEP
     LPHIEAHSVQ MSQLFYNLLS NALKFTKAGQ VPEVKVSCAL ADPALLEAQH LKGSGTYYHL
     RFSDNGIGFL NDYAQQIFTI FQRLHNRSTY EGTGIGLALC KKVVVNHHGA IYAEGEEDKG
     ATFHVLLPEK QGAI
//
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